C/EBP proteins physically interact with GABPα. (A) In vitro-translated 35S-C/EBPα protein was mixed with GST alone (lane 2), GST-fused GABPα protein (lane 3), and GST-fused GABPβ protein (lane 4). The proteins bound to each GST-fusion protein beads were analyzed by SDS-PAGE and autoradiography (top); lane 1 shows 5% of the input 35S-C/EBPα; the molecular weight markers (Prestained SDS-PAGE Standard; Bio-Rad) are shown (left). The input GST-fused proteins were analyzed by SDS-PAGE and Coomassie blue staining (bottom); the molecular weight markers are shown in lane 1. (B) In vitro-translated 35S-C/EBPβ protein was mixed with GST alone (lane 2) and GST-fused GABPα protein (lane 3). The proteins bound to each GST-fusion protein beads were analyzed by SDS-PAGE and autoradiography (top): lane 1 shows 5% of the input 35S-C/EBPβ; the molecular weight markers (Prestained SDS-PAGE Standard; Bio-Rad) are shown (left). The input GST-fused proteins were analyzed by SDS-PAGE and Coomassie blue staining (bottom); the molecular weight markers are shown in lane 1. (C) Schematic structure of GST-fused GABPα deletion mutants. ETS domain indicates E26 transformation-specific domain. (D) In vitro-translated 35S-C/EBPα protein was mixed with GST-fused GABPα protein (lane 2), the indicated GST-fused GABPα deletion mutants (lanes 3-5), and GST alone (lane 6). The proteins bound to each GST-fusion protein beads were analyzed by SDS-PAGE and autoradiography (top); lane 1 shows 5% of the input 35S-C/EBPα. The input GST-fused proteins were analyzed by SDS-PAGE and Coomassie blue staining (bottom); the molecular weight markers are shown in lane 1.
